The Need

In the field of mass spectrometry (MS), the study of proteins and protein complexes in their native form, known as native MS, has become crucial in understanding their structure and function. However, the current collision-induced dissociation (CID) technique used in tandem MS experiments can cause loss of connectivity information between protein subunits. To address this limitation, there is a commercial need for a fragmentation technique that allows for the study of protein complex topology and connectivity while preserving the native-like structure.

The Technology

The Surface-Induced Dissociation (SID) technology offers a groundbreaking solution to the limitations of current CID techniques. SID involves accelerating ions into a high mass surface to deposit a high amount of energy, enabling access to alternative dissociation pathways. These pathways allow for consistent dissociation of noncovalent proteins in patterns reflective of their native structure. SID produces subcomplexes with native-like structure and symmetrical charge distribution, providing valuable information about the connectivity and topology of intact protein complexes.

Commercial Applications

• Protein Complex Topology Analysis: SID allows researchers to characterize the topology of protein complexes, providing valuable insights into their structural organization and connectivity.

• Ligand Localization Studies: Pharmaceutical companies can use SID to identify the precise location of ligands within a protein complex, aiding in drug binding studies and drug development efforts.

• Structural Information from Low Sample Amounts: SID can be applied to obtain structural information about protein complexes from low sample amounts, enabling fast experiments and complementing other techniques like NMR and cryo-EM.

• Comparison with Crystal Structures: SID proves to be an excellent tool for comparing crystal structures with solution structures, allowing researchers to identify changes that occur during the crystal-growing process.

• Substructure Elucidation: SID can effectively elucidate the substructure of noncovalent protein complexes, aiding in understanding their functional mechanisms.

Benefits/Advantages

• Preservation of Native Structure: SID retains the native-like structure of macromolecular complexes, providing more accurate insights into their behavior in the gas phase.

• Consistent Connectivity Information: Unlike traditional CID methods, SID offers consistent and reliable connectivity information between protein subunits, enhancing the understanding of protein complex topology.

• Suitable for Low Sample Amounts: SID is capable of providing valuable structural information from small sample quantities, making it an efficient tool for high-throughput experiments.

• Pharmaceutical Relevance: With its ability to identify ligand localization within protein complexes, SID proves highly relevant to pharmaceutical companies conducting drug binding studies.

• Complementary to Existing Techniques: SID complements other structural biology techniques like NMR and cryo-EM, enhancing the overall understanding of macromolecular complexes.

In summary, the Surface-Induced Dissociation (SID) technology presents a groundbreaking solution for studying protein complex topology and connectivity while preserving their native-like structure. With applications ranging from pharmaceutical research to structural biology, SID offers significant advantages over existing techniques, making it a desirable and valuable technology for commercialization.